期刊
ELIFE
卷 10, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.58741
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- NOMIS Stiftung Svante Paabo
- Max-Planck-Gesellschaft Svante Paabo
- Bonfils-Stanton Foundation David Patterson
- Denver Foundation
Analysis of the metabolomes of humans, chimpanzees, and macaques revealed differences in the concentrations of certain metabolites, particularly those downstream of adenylosuccinate lyase. The human-specific amino acid substitution in this enzyme is believed to contribute to the reduced de novo synthesis of purines in humans.
We analyze the metabolomes of humans, chimpanzees, and macaques in muscle, kidney and three different regions of the brain. Although several compounds in amino acid metabolism occur at either higher or lower concentrations in humans than in the other primates, metabolites downstream of adenylosuccinate lyase, which catalyzes two reactions in purine synthesis, occur at lower concentrations in humans. This enzyme carries an amino acid substitution that is present in all humans today but absent in Neandertals. By introducing the modern human substitution into the genomes of mice, as well as the ancestral, Neandertal-like substitution into the genomes of human cells, we show that this amino acid substitution contributes to much or all of the reduction of de novo synthesis of purines in humans.
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